scholarly journals Six amino acid substitutions in the carboxyl-transferase domain of the plastidic acetyl-CoA carboxylase gene are linked with resistance to herbicides in a Lolium rigidum population

2006 ◽  
Vol 172 (4) ◽  
pp. 636-645 ◽  
Author(s):  
Xiao-Qi Zhang ◽  
Stephen B. Powles
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitutions ◽  
Acetyl Coa Carboxylase ◽  
Lolium Rigidum ◽  
Acetyl Coa ◽  
Resistance To Herbicides

Cross-resistance Patterns to Acetyl-CoA Carboxylase Inhibitors Associated with Different Mutations in Japanese Foxtail (Alopecurus japonicus)

Weed Science ◽  
2017 ◽  
Vol 65 (4) ◽  
pp. 444-451 ◽  
Author(s):  
Guoqi Chen ◽  
Lingyue Wang ◽  
Hongle Xu ◽  
Xibao Wu ◽  
Lang Pan ◽  
...  
Keyword(s):  
Amino Acid ◽  
Eastern China ◽  
Cross Resistance ◽  
Amino Acid Substitutions ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Cleaved Amplified Polymorphic Sequence ◽  
Resistance Patterns ◽  
Grass Weed ◽  
Clodinafop Propargyl

Japanese foxtail is a grass weed in eastern China. This weed is controlled by fenoxaprop-P-ethyl, one of the most common acetyl-CoA carboxylase (ACCase)-inhibiting herbicides. Some Japanese foxtail populations have developed resistance to fenoxaprop-P-ethyl, owing to target-site mutations (amino acid substitutions) located within the carboxyl transferase domain of ACCase. In the present study, three mutations were detected in three fenoxaprop-P-ethyl–resistant Japanese foxtail populations: Ile-1781-Leu in JCJT-2, Ile-2041-Asn in JZJR-1, and Asp-2078-Gly in JCWJ-3. Two copies ofACCase(Acc1-1andAcc1-2) were identified, but mutations were detected only inAcc1-1. The derived cleaved amplified polymorphic sequence (dCAPS) method detected these mutations successfully in Japanese foxtail. The mutation frequencies in JCJT-2, JZJR-1, and JCWJ-3 were approximately 98%, 92%, and 87%, respectively. Different cross-resistance patterns to ACCase inhibitors were found in the three resistant populations. JCJT-2 (Ile-1781-Leu) and JZJR-1 (Ile-2041-Asn) showed cross-resistance to haloxyfop-R-methyl, clodinafop-propargyl, and pinoxaden, but were susceptible to clethodim. JCWJ-3 (Asp-2078-Gly) showed cross-resistance to all tested ACCase-inhibiting herbicides.

scholarly journals Biochemical and structural characterization of quizalofop-resistant wheat acetyl-CoA carboxylase

2022 ◽  
Vol 12 (1) ◽  
Author(s):  
Raven Bough ◽  
Franck E. Dayan
Keyword(s):  
Amino Acid ◽  
Winter Wheat ◽  
Amino Acid Substitution ◽  
Reference Sequence ◽  
Cross Resistance ◽  
Homozygous Mutation ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Nucleotide Mutation

AbstractA novel nucleotide mutation in ACC1 resulting in an alanine to valine amino acid substitution in acetyl-CoA carboxylase (ACCase) at position 2004 of the Alopecurus myosuroides reference sequence (A2004V) imparts quizalofop resistance in wheat. Genotypes endowed with the homozygous mutation in one or two ACC1 homoeologs are seven- and 68-fold more resistant to quizalofop than a wildtype winter wheat in greenhouse experiments, respectively. In vitro ACCase activities in soluble protein extracts from these varieties are 3.8- and 39.4-fold more resistant to quizalofop with the homozygous mutation in either one or two genomes, relative to the wildtype. The A2004V mutation does not alter the specific activity of wheat ACCase, suggesting that this resistance trait does not affect the catalytic functions of ACCase. Modeling of wildtype and quizalofop-resistant wheat ACCase demonstrates that the A2004V amino acid substitution causes a reduction in the volume of the binding pocket that hinders quizalofop’s interaction with ACCase. Docking studies confirm that the mutation reduces the binding affinity of quizalofop. Interestingly, the models suggest that the A2004V mutation does not affect haloxyfop binding. Follow up in vivo and in vitro experiments reveal that the mutation, in fact, imparts negative cross-resistance to haloxyfop, with quizalofop-resistant varieties exhibiting higher sensitivity to haloxyfop than the wildtype winter wheat line.

Molecular basis of multiple resistance to herbicides inhibiting acetyl-CoA carboxylase and acetolactate synthase in American sloughgrass (Beckmannia syzigachne) from China

2016 ◽  
Vol 67 (11) ◽  
pp. 1208 ◽  
Author(s):  
Lang Pan ◽  
Haitao Gao ◽  
Han Wu ◽  
Liyao Dong
Keyword(s):  
Acetolactate Synthase ◽  
Alternative Methods ◽  
Multiple Resistance ◽  
Homozygous Mutation ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Wheat Field ◽  
Sequence Method ◽  
Resistance To Herbicides ◽  
Als Inhibitors

American sloughgrass (Beckmannia syzigachne Steud.) is a problematic grass that is widely distributed in wheat and oilseed rape fields in China. The herbicides fenoxaprop-P-ethyl and mesosulfuron-methyl failed to control B. syzigachne JCWJ-R populations collected from a wheat field in Jiangsu Province. Dose-response experiments showed that JCWJ-R was resistant to the acetyl-CoA carboxylase (ACCase) inhibitors fenoxaprop-P-ethyl (33.8-fold), haloxyfop-R-methyl (12.7-fold), clethodim (7.8-fold) and pinoxaden (11.6-fold), and to the acetolactate synthase (ALS) inhibitors mesosulfuron-methyl (15.9-fold), pyroxsulam (17.6-fold), flucarbazone-Na (10.7-fold) and imazethapyr (7-fold). Resistance to ALS inhibitors was due to a Pro-197-Ser mutation in the ALS gene and resistance to ACCase inhibitors was due to an Ile-1781-Leu mutation in the ACCase gene. A derived cleaved amplified polymorphic sequence method was developed to detect the ALS mutation in B. syzigachne. This was combined with a previously established method to detect Ile-1781-Leu, and the mutation frequency and homozygous mutation rates in the JCWJ-R population were determined. The evolution of multiple resistance to ACCase and ALS inhibitors in this B. syzigachne population indicated that alternative methods should be developed to control resistant weeds.

scholarly journals Biochemical and Structural Characterization of Quizalofop-Resistant Wheat Acetyl-Coa Carboxylase

2021 ◽  
Author(s):  
Raven Bough ◽  
Franck Dayan
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Specific Activity ◽  
Reference Sequence ◽  
Cross Resistance ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Nucleotide Mutation

Abstract A novel nucleotide mutation in ACC1 resulting in an alanine to valine amino acid substitution in acetyl-CoA carboxylase (ACCase) at position 2004 of the Alopecurus myosuroides reference sequence (A2004V) imparts quizalofop resistance in wheat. Genotypes endowed with one or two homozygous mutant ACC1 homoelogs are 7- and 68-fold more resistant to quizalofop than a wildtype variety in greenhouse experiments, respectively. In vitro assays of ACCase activities in protein extracts from these varieties reveal a 3.8- and 39.4-fold increase in resistance to quizalofop in the single and double-mutants relative to the wildtype. The A2004V mutation does not alter the specific activity of wheat ACCase, suggesting that ACCase mutants retain their normal catalytic functions. Modeling of wildtype and quizalofop-resistant wheat ACCase demonstrates that the A2004V amino acid substitution causes a reduction in the volume of the binding pocket that hinders quizalofop’s interaction with ACCase. Docking studies confirm that the mutation reduces the binding affinity of quizalofop. Interestingly, the models suggest that the A2004V mutation does not affect haloxyfop binding. Follow up in vivo and in vitro experiments reveal that the mutation, in fact, imparts negative cross-resistance to haloxyfop, with quizalofop-resistant varieties exhibiting more sensitivity to haloxyfop than the wildtype variety.

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